Q9UIG0 (BAZ1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase BAZ1B
EC=2.7.10.2

Alternative name(s):
Bromodomain adjacent to zinc finger domain protein 1B
Williams syndrome transcription factor
Williams-Beuren syndrome chromosomal region 10 protein
Williams-Beuren syndrome chromosomal region 9 protein
hWALp2

Gene names

Name:	BAZ1B
Synonyms:	WBSC10, WBSCR10, WBSCR9, WSTF

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1483 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. In the WINAC complex, plays an essential role by targeting the complex to acetylated histones, an essential step for VDR-promoter association. Ref.7 Ref.8 Ref.9 Ref.12 Ref.16 Ref.17
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.16
Cofactor	Manganese. Ref.16
Subunit structure	Interacts with MYO1C By similarity. Interacts with CDT1. Interacts with SMARCA5/SNF2H; the interaction is direct and forms the WICH complex. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with VDR; in a ligand-dependent manner. Interacts with PCNA; the interaction is direct. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13
Subcellular location	Nucleus. Note: Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA. Ref.7 Ref.9
Tissue specificity	Ubiquitously expressed with high levels of expression in heart, brain, placenta, skeletal muscle and ovary.
Developmental stage	Expressed at equal levels in 19-23 weeks old fetal tissues.
Domain	The N-terminal part (1-345), including the WAC domain and the C motif, mediates the tyrosine-protein kinase activity. Ref.10 The bromo domain mediates the specific interaction with acetylated histones. Ref.10
Involvement in disease	BAZ1B is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of BAZ1B may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease. Ref.2
Sequence similarities	Belongs to the WAL family. BAZ1B subfamily. Contains 1 bromo domain. Contains 1 DDT domain. Contains 1 PHD-type zinc finger. Contains 1 WAC domain.
Sequence caution	The sequence AAC97879.1 differs from that shown. Reason: Frameshift at positions 1031, 1042 and 1422. The sequence AAD04720.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAH65029.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence BAA89210.1 differs from that shown. Reason: Frameshift at position 1478.

Ontologies

Keywords
Biological process	DNA damage Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Williams-Beuren syndrome
Domain	Bromodomain Coiled coil Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP-dependent chromatin remodeling Inferred from direct assay Ref.8. Source: BHF-UCL DNA replication-dependent nucleosome disassembly Inferred from mutant phenotype Ref.8. Source: BHF-UCL chromatin-mediated maintenance of transcription Inferred from sequence or structural similarity. Source: BHF-UCL double-strand break repair Inferred from sequence or structural similarity. Source: BHF-UCL heart morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL transcription, DNA-dependent Non-traceable author statement Ref.3. Source: BHF-UCL
Cellular_component	WINAC complex Inferred from direct assay Ref.8. Source: BHF-UCL centromeric heterochromatin Inferred from electronic annotation. Source: Compara condensed chromosome Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from direct assay Ref.10. Source: UniProtKB histone acetyl-lysine binding Inferred from direct assay Ref.10. Source: UniProtKB histone kinase activity Inferred from direct assay Ref.16. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein complex scaffold Inferred from direct assay Ref.8. Source: BHF-UCL protein tyrosine kinase activity Inferred from direct assay Ref.16. Source: UniProtKB vitamin D receptor activator activity Inferred from mutant phenotype Ref.8. Source: BHF-UCL zinc ion binding Non-traceable author statement Ref.21. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMARCA5	O60264	6	EBI-927482,EBI-352588

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UIG0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UIG0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     660-663: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1483

1483

Tyrosine-protein kinase BAZ1B

PRO_0000211170

Regions

Domain

20 – 126

107

WAC

Domain

604 – 668

65

DDT

Domain

1356 – 1426

71

Bromo

Zinc finger

1184 – 1234

51

PHD-type

Region

1 – 345

345

Mediates the tyrosine-protein kinase activity

Coiled coil

533 – 586

54

Potential

Coiled coil

768 – 814

47

Potential

Coiled coil

850 – 893

44

Potential

Coiled coil

1245 – 1283

39

Potential

Motif

207 – 213

7

C motif

Compositional bias

306 – 578

273

Lys-rich

Compositional bias

1261 – 1273

13

Poly-Glu

Amino acid modifications

Modified residue

161

1

Phosphoserine By similarity

Modified residue

266

1

Phosphothreonine Ref.19

Modified residue

283

1

Phosphoserine By similarity

Modified residue

330

1

Phosphoserine Ref.15

Modified residue

345

1

Phosphoserine Ref.19

Modified residue

347

1

Phosphoserine Ref.19 Ref.20

Modified residue

349

1

Phosphoserine Ref.19 Ref.20

Modified residue

361

1

Phosphoserine Ref.19

Modified residue

374

1

Phosphoserine Ref.15

Modified residue

699

1

Phosphoserine Ref.15

Modified residue

705

1

Phosphoserine Ref.15 Ref.18 Ref.20

Modified residue

708

1

Phosphoserine Ref.15

Modified residue

716

1

Phosphoserine Ref.15

Modified residue

947

1

Phosphoserine Ref.15

Modified residue

1315

1

Phosphoserine Ref.15

Modified residue

1342

1

Phosphoserine Ref.11 Ref.19 Ref.20

Modified residue

1468

1

Phosphoserine Ref.11 Ref.14 Ref.15 Ref.19 Ref.20

Natural variations

Alternative sequence

660 – 663

4

Missing in isoform 2.

VSP_000552

Experimental info

Mutagenesis

338

1

C → A: Loss of tyrosine-protein kinase activity. Ref.16

Sequence conflict

14

1

K → N in BAA89210. Ref.3

Sequence conflict

22

1

L → F in BAA89210. Ref.3

Sequence conflict

136

1

K → E in AAD08675. Ref.1

Sequence conflict

823

1

E → R in BAA89210. Ref.3

Sequence conflict

1191

1

R → P in BAA89210. Ref.3

Sequence conflict

1354

1

K → M in AAC97879. Ref.2

Sequence conflict

1438

1

A → V in BAA89210. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

1483

Helix Strand Turn

Details...

Turn

1188 – 1190

3

Turn

1203 – 1205

3

Helix

1211 – 1214

4

Turn

1229 – 1231

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 30, 2002. Version 2. Checksum: 0CC146FEBB954261	FASTA	1,483	170,903
	10 20 30 40 50 60 MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL 70 80 90 100 110 120 THKEAWEEEQ EVAELLKEEF PAWYEKLVLE MVHHNTASLE KLVDTAWLEI MTKYAVGEEC 130 140 150 160 170 180 DFEVGKEKML KVKIVKIHPL EKVDEEATEK KSDGACDSPS SDKENSSQIA QDHQKKETVV 190 200 210 220 230 240 KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS 250 260 270 280 290 300 LIRTERPPNK EIVRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT 310 320 330 340 350 360 LNPSTKRKNT GSPDRKPSKK SKTDNSSLSS PLNPKLWCHV HLKKSLSGSP LKVKNSKNSK 370 380 390 400 410 420 SPEEHLEEMM KMMSPNKLHT NFHIPKKGPP AKKPGKHSDK PLKAKGRSKG ILNGQKSTGN 430 440 450 460 470 480 SKSPKKGLKT PKTKMKQMTL LDMAKGTQKM TRAPRNSGGT PRTSSKPHKH LPPAALHLIA 490 500 510 520 530 540 YYKENKDRED KRSALSCVIS KTARLLSSED RARLPEELRS LVQKRYELLE HKKRWASMSE 550 560 570 580 590 600 EQRKEYLKKK REELKKKLKE KAKERREKEM LERLEKQKRY EDQELTGKNL PAFRLVDTPE 610 620 630 640 650 660 GLPNTLFGDV AMVVEFLSCY SGLLLPDAQY PITAVSLMEA LSADKGGFLY LNRVLVILLQ 670 680 690 700 710 720 TLLQDEIAED YGELGMKLSE IPLTLHSVSE LVRLCLRRSD VQEESEGSDT DDNKDSAAFE 730 740 750 760 770 780 DNEVQDEFLE KLETSEFFEL TSEEKLQILT ALCHRILMTY SVQDHMETRQ QMSAELWKER 790 800 810 820 830 840 LAVLKEENDK KRAEKQKRKE MEAKNKENGK VENGLGKTDR KKEIVKFEPQ VDTEAEDMIS 850 860 870 880 890 900 AVKSRRLLAI QAKKEREIQE REMKVKLERQ AEEERIRKHK AAAEKAFQEG IAKAKLVMRR 910 920 930 940 950 960 TPIGTDRNHN RYWLFSDEVP GLFIEKGWVH DSIDYRFNHH CKDHTVSGDE DYCPRSKKAN 970 980 990 1000 1010 1020 LGKNASMNTQ HGTATEVAVE TTTPKQGQNL WFLCDSQKEL DELLNCLHPQ GIRESQLKER 1030 1040 1050 1060 1070 1080 LEKRYQDIIH SIHLARKPNL GLKSCDGNQE LLNFLRSDLI EVATRLQKGG LGYVEETSEF 1090 1100 1110 1120 1130 1140 EARVISLEKL KDFGECVIAL QASVIKKFLQ GFMAPKQKRR KLQSEDSAKT EEVDEEKKMV 1150 1160 1170 1180 1190 1200 EEAKVASALE KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI 1210 1220 1230 1240 1250 1260 LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPATARRNS RGRNYTEESA SEDSEDDESD 1270 1280 1290 1300 1310 1320 EEEEEEEEEE EEEDYEVAGL RLRPRKTIRG KHSVIPPAAR SGRRPGKKPH STRRSQPKAP 1330 1340 1350 1360 1370 1380 PVDDAEVDEL VLQTKRSSRR QSLELQKCEE ILHKIVKYRF SWPFREPVTR DEAEDYYDVI 1390 1400 1410 1420 1430 1440 THPMDFQTVQ NKCSCGSYRS VQEFLTDMKQ VFTNAEVYNC RGSHVLSCMV KTEQCLVALL 1450 1460 1470 1480 HKHLPGHPYV RRKRKKFPDR LAEDEGDSEP EAVGQSRGRR QKK
	Isoform 2 [UniParc]. Checksum: D0F1A5559EB52F78	FASTA	1,479	170,447
	10 20 30 40 50 60 MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL 70 80 90 100 110 120 THKEAWEEEQ EVAELLKEEF PAWYEKLVLE MVHHNTASLE KLVDTAWLEI MTKYAVGEEC 130 140 150 160 170 180 DFEVGKEKML KVKIVKIHPL EKVDEEATEK KSDGACDSPS SDKENSSQIA QDHQKKETVV 190 200 210 220 230 240 KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS 250 260 270 280 290 300 LIRTERPPNK EIVRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT 310 320 330 340 350 360 LNPSTKRKNT GSPDRKPSKK SKTDNSSLSS PLNPKLWCHV HLKKSLSGSP LKVKNSKNSK 370 380 390 400 410 420 SPEEHLEEMM KMMSPNKLHT NFHIPKKGPP AKKPGKHSDK PLKAKGRSKG ILNGQKSTGN 430 440 450 460 470 480 SKSPKKGLKT PKTKMKQMTL LDMAKGTQKM TRAPRNSGGT PRTSSKPHKH LPPAALHLIA 490 500 510 520 530 540 YYKENKDRED KRSALSCVIS KTARLLSSED RARLPEELRS LVQKRYELLE HKKRWASMSE 550 560 570 580 590 600 EQRKEYLKKK REELKKKLKE KAKERREKEM LERLEKQKRY EDQELTGKNL PAFRLVDTPE 610 620 630 640 650 660 GLPNTLFGDV AMVVEFLSCY SGLLLPDAQY PITAVSLMEA LSADKGGFLY LNRVLVILLQ 670 680 690 700 710 720 DEIAEDYGEL GMKLSEIPLT LHSVSELVRL CLRRSDVQEE SEGSDTDDNK DSAAFEDNEV 730 740 750 760 770 780 QDEFLEKLET SEFFELTSEE KLQILTALCH RILMTYSVQD HMETRQQMSA ELWKERLAVL 790 800 810 820 830 840 KEENDKKRAE KQKRKEMEAK NKENGKVENG LGKTDRKKEI VKFEPQVDTE AEDMISAVKS 850 860 870 880 890 900 RRLLAIQAKK EREIQEREMK VKLERQAEEE RIRKHKAAAE KAFQEGIAKA KLVMRRTPIG 910 920 930 940 950 960 TDRNHNRYWL FSDEVPGLFI EKGWVHDSID YRFNHHCKDH TVSGDEDYCP RSKKANLGKN 970 980 990 1000 1010 1020 ASMNTQHGTA TEVAVETTTP KQGQNLWFLC DSQKELDELL NCLHPQGIRE SQLKERLEKR 1030 1040 1050 1060 1070 1080 YQDIIHSIHL ARKPNLGLKS CDGNQELLNF LRSDLIEVAT RLQKGGLGYV EETSEFEARV 1090 1100 1110 1120 1130 1140 ISLEKLKDFG ECVIALQASV IKKFLQGFMA PKQKRRKLQS EDSAKTEEVD EEKKMVEEAK 1150 1160 1170 1180 1190 1200 VASALEKWKT AIREAQTFSR MHVLLGMLDA CIKWDMSAEN ARCKVCRKKG EDDKLILCDE 1210 1220 1230 1240 1250 1260 CNKAFHLFCL RPALYEVPDG EWQCPACQPA TARRNSRGRN YTEESASEDS EDDESDEEEE 1270 1280 1290 1300 1310 1320 EEEEEEEEED YEVAGLRLRP RKTIRGKHSV IPPAARSGRR PGKKPHSTRR SQPKAPPVDD 1330 1340 1350 1360 1370 1380 AEVDELVLQT KRSSRRQSLE LQKCEEILHK IVKYRFSWPF REPVTRDEAE DYYDVITHPM 1390 1400 1410 1420 1430 1440 DFQTVQNKCS CGSYRSVQEF LTDMKQVFTN AEVYNCRGSH VLSCMVKTEQ CLVALLHKHL 1450 1460 1470 PGHPYVRRKR KKFPDRLAED EGDSEPEAVG QSRGRRQKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of the WBSCR9 gene, encoding a novel transcriptional regulator, in the Williams-Beuren syndrome deletion at 7q11.23." Peoples R.J., Cisco M.J., Kaplan P., Francke U. Cytogenet. Cell Genet. 82:238-246(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"A novel human gene, WSTF, is deleted in Williams Syndrome." Lu X., Meng X., Morris C.A., Keating M.T. Genomics 54:241-249(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN WBS.
[3]	"A novel family of bromodomain genes." Jones M.H., Hamana N., Nezu J., Shimane M. Genomics 63:40-45(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Testis.
[4]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[7]	"WSTF-ISWI chromatin remodeling complex targets heterochromatic replication foci." Bozhenok L., Wade P.A., Varga-Weisz P. EMBO J. 21:2231-2241(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome." Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S. Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[9]	"The Williams syndrome transcription factor interacts with PCNA to target chromatin remodelling by ISWI to replication foci." Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S., Ferreira F., Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D. Nat. Cell Biol. 6:1236-1244(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA.
[10]	"Ligand-induced transrepression by VDR through association of WSTF with acetylated histones." Fujiki R., Kim M.-S., Sasaki Y., Yoshimura K., Kitagawa H., Kato S. EMBO J. 24:3881-3894(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VDR, DOMAIN BROMO.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1342 AND SER-1468, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription." Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K. J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE B-WICH COMPLEX.
[13]	"Identification of novel human Cdt1-binding proteins by a proteomics approach: proteolytic regulation by APC/CCdh1." Sugimoto N., Kitabayashi I., Osano S., Tatsumi Y., Yugawa T., Narisawa-Saito M., Matsukage A., Kiyono T., Fujita M. Mol. Biol. Cell 19:1007-1021(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CDT1.
[14]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1468, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-374; SER-699; SER-705; SER-708; SER-716; SER-947; SER-1315 AND SER-1468, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity." Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A., Erdjument-Bromage H., Ishibe-Murakami S., Wang B., Tempst P., Hofmann K., Patel D.J., Elledge S.J., Allis C.D. Nature 457:57-62(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF CYS-338.
[17]	"Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions." Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G. Nature 458:591-596(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-705, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266; SER-345; SER-347; SER-349; SER-361; SER-1342 AND SER-1468, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-349; SER-705; SER-1342 AND SER-1468, MASS SPECTROMETRY.
[21]	"Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor." Pascual J., Martinez-Yamout M., Dyson H.J., Wright P.E. J. Mol. Biol. 304:723-729(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1185-1235.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF084479 mRNA. Translation: AAD08675.1.
AF072810 mRNA. Translation: AAC97879.1. Frameshift.
AB032253 mRNA. Translation: BAA89210.1. Frameshift.
AC005074 Genomic DNA. Translation: AAD04720.1. Sequence problems.
AC005089 Genomic DNA. Translation: AAP22332.1.
CH471200 Genomic DNA. Translation: EAW69680.1.
CH471200 Genomic DNA. Translation: EAW69681.1.
BC065029 mRNA. Translation: AAH65029.1. Sequence problems.
BC136520 mRNA. Translation: AAI36521.1.

IPI

IPI00069817.
IPI00216695.

RefSeq

NP_115784.1. NM_032408.3.

UniGene

Hs.647016.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F62	NMR	-	A	1185-1235	[»]

ProteinModelPortal

Q9UIG0.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35642N.

IntAct

Q9UIG0. 9 interactions.

MINT

MINT-1894324.

STRING

9606.ENSP00000342434.

PTM databases

PhosphoSite

Q9UIG0.

Polymorphism databases

DMDM

22653670.

Proteomic databases

PaxDb

Q9UIG0.

PRIDE

Q9UIG0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000339594; ENSP00000342434; ENSG00000009954.
ENST00000404251; ENSP00000385442; ENSG00000009954.
ENST00000573731; ENSP00000461849; ENSG00000262694.
ENST00000575505; ENSP00000460410; ENSG00000262694.

GeneID

9031.

KEGG

hsa:9031.

UCSC

uc003tyc.3. human.

Organism-specific databases

CTD

9031.

GeneCards

GC07M072854.

HGNC

HGNC:961. BAZ1B.

HPA

CAB037158.

MIM

605681. gene.

neXtProt

NX_Q9UIG0.

Orphanet

904. Williams syndrome.

PharmGKB

PA25271.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5076.

HOVERGEN

HBG050668.

InParanoid

Q9UIG0.

KO

K11658.

OMA

CNKAFHL.

OrthoDB

EOG4MKNFK.

PhylomeDB

Q9UIG0.

Gene expression databases

Bgee

Q9UIG0.

CleanEx

HS_BAZ1B.

Genevestigator

Q9UIG0.

GermOnline

ENSG00000009954. Homo sapiens.

Family and domain databases

Gene3D

1.20.920.10. 1 hit.
3.30.40.10. 1 hit.

InterPro

IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR018500. DDT_dom_subgr.
IPR018501. DDT_dom_superfamily.
IPR013136. WSTF_Acf1_Cbp146.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Pfam

PF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF10537. WAC_Acf1_DNA_bd. 1 hit.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]

SUPFAM

SSF47370. Bromodomain. 1 hit.
SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50827. DDT. 1 hit.
PS51136. WAC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

BAZ1B. human.

EvolutionaryTrace

Q9UIG0.

GenomeRNAi

9031.

NextBio

33835.

SOURCE

Search...

Entry information

Entry name

BAZ1B_HUMAN

Accession

Primary (citable) accession number: Q9UIG0
Secondary accession number(s): B9EGK3 , D3DXE9, O95039, O95247, O95277, Q6P1K4, Q86UJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	August 30, 2002
Last modified:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.